Research workbench
Solution structure of the first C2 domain from human B/K protein
Analyse Solution structure of the first C2 domain from human B/K protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ENP
- Type
- protein
- Length
- 147 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- B/K protein
- UniProt
- Q9NZ18
- Pockets
- 1 · best druggability 0.51
Structure
solution nmr · 1 distinct chain · 4% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | B/K protein | protein | 147 | 4% helix, 33% strand | Q9NZ18 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.51 | 0.81 | 29 | empty |
Compared structures
- 2ENP · Solution structure of the first C2 domain from human B/K protein · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9NZ18
- Elsewhere: RCSB PDB 2ENP · PDBe 2ENP · UniProt Q9NZ18
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